Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

@article{Holley2002ReaperEI,
  title={Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition},
  author={Christopher L. Holley and Michael R. Olson and Daniel Col{\'o}n-Ramos and Sally Kornbluth},
  journal={Nature Cell Biology},
  year={2002},
  volume={40},
  pages={439-444}
}
Inhibitors of apoptosis (IAPs) inhibit caspases, thereby preventing proteolysis of apoptotic substrates. IAPs occlude the active sites of caspases to which they are bound and can function as ubiquitin ligases. IAPs are also reported to ubiquitinate themselves and caspases. Several proteins induce apoptosis, at least in part, by binding and inhibiting IAPs. Among these are the Drosophila melanogaster proteins Reaper (Rpr), Grim, and HID, and the mammalian proteins Smac/Diablo and Omi/HtrA2, all… CONTINUE READING

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